SPO24_YEAST
ID SPO24_YEAST Reviewed; 67 AA.
AC Q3E752; D6W447;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Sporulation protein 24 {ECO:0000303|PubMed:25127041};
GN Name=SPO24 {ECO:0000303|PubMed:25127041, ECO:0000312|SGD:S000028425};
GN OrderedLocusNames=YPR036W-A {ECO:0000312|SGD:S000028425};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INDUCTION.
RX PubMed=11557050; DOI=10.1016/s0014-5793(01)02792-2;
RA Miura F., Yada T., Nakai K., Sakaki Y., Ito T.;
RT "Differential display analysis of mutants for the transcription factor
RT Pdr1p regulating multidrug resistance in the budding yeast.";
RL FEBS Lett. 505:103-108(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-32, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25127041; DOI=10.1371/journal.pone.0105058;
RA Hurtado S., Kim Guisbert K.S., Sontheimer E.J.;
RT "SPO24 is a transcriptionally dynamic, small ORF-encoding locus required
RT for efficient sporulation in Saccharomyces cerevisiae.";
RL PLoS ONE 9:E105058-E105058(2014).
CC -!- FUNCTION: Required for efficient sporulation.
CC {ECO:0000269|PubMed:25127041}.
CC -!- SUBCELLULAR LOCATION: Prospore membrane {ECO:0000269|PubMed:25127041};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- INDUCTION: By PDR1 through its PDRE-like promoter element.
CC {ECO:0000269|PubMed:11557050}.
CC -!- PTM: Phosphorylated during meiosis. During meiosis, exists in both
CC unphosphorylated and phosphorylated forms with the highest degree of
CC phosphorylation occurring in mid-meiosis.
CC {ECO:0000269|PubMed:25127041}.
CC -!- DISRUPTION PHENOTYPE: Defective sporulation accompanied by the
CC appearance of pseudohyphal-like projections.
CC {ECO:0000269|PubMed:25127041}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z68111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006949; DAA11463.1; -; Genomic_DNA.
DR RefSeq; NP_690847.1; NM_001184516.1.
DR AlphaFoldDB; Q3E752; -.
DR BioGRID; 36215; 75.
DR STRING; 4932.YPR036W-A; -.
DR iPTMnet; Q3E752; -.
DR PaxDb; Q3E752; -.
DR PRIDE; Q3E752; -.
DR EnsemblFungi; YPR036W-A_mRNA; YPR036W-A; YPR036W-A.
DR GeneID; 856149; -.
DR KEGG; sce:YPR036W-A; -.
DR SGD; S000028425; SPO24.
DR VEuPathDB; FungiDB:YPR036W-A; -.
DR eggNOG; ENOG502SF97; Eukaryota.
DR HOGENOM; CLU_195455_0_0_1; -.
DR InParanoid; Q3E752; -.
DR OMA; NSCASDY; -.
DR BioCyc; YEAST:G3O-34361-MON; -.
DR ChiTaRS; SPO24; yeast.
DR PRO; PR:Q3E752; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q3E752; protein.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Sporulation.
FT CHAIN 1..67
FT /note="Sporulation protein 24"
FT /id="PRO_0000242699"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 67 AA; 7055 MW; 1D9B827BE611C6B5 CRC64;
MVAFLELTSD VSQPFVIPSL SPVSQPSSRK NSDANVDDLN LAIANAALLD ASASSRSHSR
KNSLSLL
